2Z6K: Full-length human RPA14/32 heterodimer

Crystal structure of full-length human RPA14/32 heterodimer. Determined by X-ray diffraction at 3.0 Å resolution. Released 4 Dec 2007.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,818
Mol. weight: 90.79 kDa
Released: 4 Dec 2007

Explore 2Z6K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Z6K contains 17 α-helices and 30 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	47-48	2	1
α-helix	51-56	6
β-strand	58-59	2	2
β-strand	64-66	3	2
β-strand	69-71	3	2
β-strand	73-82	10	1
β-strand	89-95	7	1
β-strand	102-107	6	1
α-helix	118-121	4
β-strand	125-134	10	1
β-strand	139-148	10	1
α-helix	153-172	20

Chain B: 3 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	46-48	3	3
α-helix	51-55	5
β-strand	58	1	4
β-strand	64-66	3	4
β-strand	69-71	3	4
β-strand	73-80	8	3
β-strand	90-95	6	3
β-strand	102-106	5	3
α-helix	119-121	3
β-strand	125-133	9	3
β-strand	140-148	9	3
α-helix	153-171	19

Chain C: 5 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
β-strand	10-12	3	5
α-helix	14-16	3
α-helix	18-20	3
β-strand	24-34	11	5
β-strand	40-44	5	5
β-strand	50-54	5	5
α-helix	58-59	2
β-strand	66-73	8	5
β-strand	79-86	8	5
α-helix	96-108	13

Chain D: 6 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
β-strand	10-12	3	6
α-helix	14-20	7
β-strand	24-34	11	6
α-helix	35	1
β-strand	40-44	5	6
β-strand	50-54	5	6
β-strand	66-73	8	6
β-strand	79-86	8	6
α-helix	87-88	2
α-helix	93-95	3
α-helix	96-108	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Replication protein A 32 kDa subunit	A, B	protein	270	Homo sapiens	P15927 (AlphaFold model)
Replication protein A 14 kDa subunit	C, D	protein	142	Homo sapiens	P35244 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2Z6K_1 Replication protein A 32 kDa subunit (chains A, B)
MWNSGFESYGSSSYGGAGGYTQSPGGFGSPAPSQAEKKSRARAQHIVPCTISQLLSATLV
DEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSSENTVV
PPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAGR
APISNPGMSEAGNFGGNSFMPANGLTVAQNQVLNLIKACPRPEGLNFQDLKNQLKHMSVS
SIKQAVDFLSNEGHIYSTVDDDHFKSTDAE

Sequence of entity 2 (C, D), FASTA

>2Z6K_2 Replication protein A 14 kDa subunit (chains C, D)
MGHHHHHHHHHHSSGHIEGRHMVDMMDLPRSRINAGMLAQFIDKPVCFVGRLEKIHPTGK
MFILSDGEGKNGTIELMEPLDEEISGIVEVVGRVTAKATILCTSYVQFKEDSHPFDLGLY
NEAVKIIHDFPQFYPLGIVQHD

Primary citation

Structure of the Full-length Human RPA14/32 Complex Gives Insights into the Mechanism of DNA Binding and Complex Formation. Deng, X., Habel, J.E., Kabaleeswaran, V. et al. J Mol Biol (2007) 374:865-876. DOI 10.1016/j.jmb.2007.09.074 · PubMed

Other PDB entries of the same protein (UniProt P15927 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4OU0 1.4 Å, Crystal Structure of RPA32C
4MQV 1.95 Å, Crystal complex of Rpa32c and Smarcal1 N-terminus
3KDF 1.98 Å, X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell…
2PI2 2.0 Å, Full-length Replication protein A subunits RPA14 and RPA32
1QUQ 2.5 Å, Complex of replication protein A subunits RPA14 and RPA32
2PQA 2.5 Å, Crystal Structure of Full-length Human RPA 14/32 Heterodimer
1L1O 2.8 Å, Structure of the human Replication Protein A (RPA) trimerization core
8RK2 3.2 Å, Human Replication protein A (RPA; trimeric core) - ssDNA complex
9PD3 3.3 Å, NER dual incision complex - DuIS
9PD4 3.4 Å, NER dual incision complex - DuIM
9MJ5 3.5 Å, Catalytic domain of human DNA polymerase alpha in complex with DNA and RPA
1DPU Solution structure of the C-terminal domain of human RPA32 complexed with UNG2(73-88)

Browse structure collections

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